ID A0A0R2I7P1_CARDV Unreviewed; 494 AA.
AC A0A0R2I7P1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=IV74_GL001298 {ECO:0000313|EMBL:KRN58039.1};
OS Carnobacterium divergens DSM 20623.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Carnobacterium.
OX NCBI_TaxID=1449336 {ECO:0000313|EMBL:KRN58039.1, ECO:0000313|Proteomes:UP000051658};
RN [1] {ECO:0000313|EMBL:KRN58039.1, ECO:0000313|Proteomes:UP000051658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20623 {ECO:0000313|EMBL:KRN58039.1,
RC ECO:0000313|Proteomes:UP000051658};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000256|ARBA:ARBA00009121}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRN58039.1}.
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DR EMBL; JQBS01000001; KRN58039.1; -; Genomic_DNA.
DR RefSeq; WP_034568174.1; NZ_JQLO01000001.1.
DR AlphaFoldDB; A0A0R2I7P1; -.
DR PATRIC; fig|1449336.4.peg.1324; -.
DR eggNOG; COG3469; Bacteria.
DR eggNOG; COG3979; Bacteria.
DR Proteomes; UP000051658; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd12215; ChiC_BD; 1.
DR CDD; cd00063; FN3; 1.
DR CDD; cd02871; GH18_chitinase_D-like; 1.
DR Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR003610; CBM_fam5/12.
DR InterPro; IPR036573; CBM_sf_5/12.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR45708; ENDOCHITINASE; 1.
DR PANTHER; PTHR45708:SF49; ENDOCHITINASE; 1.
DR Pfam; PF02839; CBM_5_12; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00495; ChtBD3; 1.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51055; Carbohydrate binding domain; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023024};
KW Chitin degradation {ECO:0000256|ARBA:ARBA00023024};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023024};
KW Reference proteome {ECO:0000313|Proteomes:UP000051658};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..494
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006418191"
FT DOMAIN 44..336
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 360..445
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
SQ SEQUENCE 494 AA; 53652 MW; 640D6CF6F0B6192C CRC64;
MKKGNLFKKG LILGVTACSL FLVQQLKVNA ADDASVMPSI ENKQILMGFW HNWQANPNDG
YKRGSSAEIA LRDTPDAYNV VAVAFMKGEG IPTFKPYKGT DAEFRQQVGE LNKAGKPVLI
SLGGADAHVQ LKNGDETAFA NELIRLVETY GFDGIDIDLE QAAITAGDNK TVIPKALKIV
KAHYKAQNQN FIISMAPEFP YLKPGNAYES YLTSLKDEYD FIAPQLYNQG GDGVWVDEIS
KWVTQNDDAY KYEFLYYMAD SLIHGTRGFL QIPASKLAIG LPANNDAGAS GYVKDPQVVY
NVFDQLKKDG NPIKGLMTWS INWDLGKDVN GVAYNQGFSK AYDTLINGGG GVADTEKPSA
PTNVKASNIT ANQVQLDWTA STDNIGVTGY QILRDGVVVG TAKGTTYSDS GLKPATSYSY
QIKATDRAGN VSLGSASLAV KTIEGPEVPS NEWDATKTYV AGDKVTYKGK GYQAQWWTKG
EEPSLATSIV WKAI
//
